CYTIP Human

Cytohesin 1 Interacting Protein Human Recombinant
Cat. No.
BT27473
Source
E.coli.
Synonyms
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CYTIP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-359 a.a) and having a molecular mass of 42.6kDa.
CYTIP is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Cytohesin-interacting protein, also known as CYTIP, is a protein that contains two leucine zipper domains and a possible nuclear targeting signal at the C-terminal. Notably, CYTIP lacks hydrophobic regions. CYTIP is expressed at low levels in resting NK and T cells and is involved in regulating the activation of ARF genes by CYTH1.
Description
Recombinant human CYTIP, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 384 amino acids (amino acids 1-359). It has a molecular weight of 42.6 kDa. The CYTIP protein is fused to a 25 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
CYTIP protein solution (1 mg/ml) in a buffer containing 20 mM Tris-HCl (pH 8.0) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For longer storage, freeze the product at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the protein is greater than 85% as determined by SDS-PAGE analysis.
Synonyms
Cytohesin 1 Interacting Protein, Cytohesin Binder And Regulator, PSCDBP, Pleckstrin Homology, Sec7 And Coiled-Coil Domains, Binding Protein,Pleckstrin Homology Sec7 And Coiled-Coil Domains-Binding Protein, Cytohesin-Associated Scaffolding Protein, Cytohesin Binding Protein HE, Cytohesin-Binding Protein HE, Cbp HE, CASP, CYBR, HE Pleckstrin Homology, Sec7 And Coiled/Coil Domains, Binding Protein, Cytohesin-1 Interacting Protein, Cytohesin-Interacting Protein, CYTHIP, B3-1, CYTIP.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPPGSH MGSEFMSLQR LLQHSSNGNL ADFCAGPAYS SYSTLTGSLT MDDNRRIQML ADTVATLPRG RKQLALTRSS SLSDFSWSQR KLVTVEKQDN ETFGFEIQSY RPQNQNACSS EMFTLICKIQ EDSPAHCAGL QAGDVLANIN GVSTEGFTYK QVVDLIRSSG NLLTIETLNG TMILKRTELE AKLQVLKQTL KQKWVEYRSL QLQEHRLLHG DAANCPSLEN MDLDELSLFG PLPGPGPALV DRNRLSSESS CKSWLSSMTM DSEDGYQTCV SEDSSRGAFS RQTSTDDECF IPKEGDDFLR RSSSRRNRSI SNTSSGSMSP LWEGNLSSMF GTLPRKSRKG SVRKQLLKFI PGLHRAVEEE ESRF

Product Science Overview

Introduction

Cytohesin 1 Interacting Protein, also known as CYTH1, is a crucial mediator of cell adhesion and migration. It plays a significant role in various cellular processes, particularly in the immune system and hematopoietic stem cells (HSPCs). This article delves into the background, structure, function, and significance of CYTH1 in human biology.

Structure and Function

CYTH1 is a guanine nucleotide exchange factor (GEF) that primarily interacts with the small GTPase ARF (ADP-ribosylation factor) family. It is involved in the activation of integrins, which are essential for cell adhesion and migration. Integrins are transmembrane receptors that facilitate cell-extracellular matrix (ECM) adhesion. CYTH1 specifically regulates the activation of integrin β1 and β2 subunits, which are crucial for the adhesion and migration of various cell types, including hematopoietic stem cells and dendritic cells .

Role in Hematopoietic Stem Cells

CYTH1 has been identified as a critical mediator of adhesive properties in primary human cord blood-derived hematopoietic stem and progenitor cells (HSPCs). Knockdown of CYTH1 disrupts the adhesion of HSPCs to primary human mesenchymal stroma cells, impairing their attachment to fibronectin and ICAM1, two integrin ligands. This disruption leads to a reduced integrin β1 activation response, suggesting that CYTH1 mediates integrin-dependent functions .

Transplantation studies have shown that CYTH1-knockdown cells exhibit significantly lower long-term engraftment levels, associated with a reduced capacity to home to the bone marrow. Intravital microscopy has revealed that CYTH1 deficiency profoundly affects HSPC mobility and localization within the marrow space, impairing proper lodgment into the niche .

Role in Dendritic Cells

In dendritic cells, CYTH1 controls the activation of RhoA, a small GTPase, and modulates integrin-dependent adhesion and migration. CYTH1 and RhoA are both required for the induction of chemokine-dependent conformational changes of the integrin β2 subunit during adhesion under physiological flow conditions. Interference with CYTH1 signaling impairs the migration of dendritic cells in complex 3D environments and in vivo .

Significance in Immune Response

Integrin-mediated adhesion is essential for various immune defense mechanisms. CYTH1 plays a pivotal role in the rapid adhesion of leukocytes to activated endothelia, a process crucial for immune cell egress from the vasculature into lymphoid organs or infected tissues. The activation of integrins by CYTH1 involves both direct interactions and signal transduction through its GEF domain, which activates ARF GTPases .

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